ID A0A1W9J9H9_9PROT Unreviewed; 654 AA.
AC A0A1W9J9H9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptidoglycan D,D-transpeptidase MrdA {ECO:0000256|HAMAP-Rule:MF_02081};
DE EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02081};
DE AltName: Full=Penicillin-binding protein 2 {ECO:0000256|HAMAP-Rule:MF_02081};
DE Short=PBP-2 {ECO:0000256|HAMAP-Rule:MF_02081};
GN Name=mrdA {ECO:0000256|HAMAP-Rule:MF_02081};
GN ORFNames=BVN34_07675 {ECO:0000313|EMBL:OQW68568.1};
OS Proteobacteria bacterium ST_bin12.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978760 {ECO:0000313|EMBL:OQW68568.1, ECO:0000313|Proteomes:UP000192616};
RN [1] {ECO:0000313|EMBL:OQW68568.1, ECO:0000313|Proteomes:UP000192616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin12 {ECO:0000313|EMBL:OQW68568.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02081};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02081}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02081}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02081}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQW68568.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSXP01000006; OQW68568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9J9H9; -.
DR STRING; 1978760.BVN34_07675; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000192616; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR HAMAP; MF_02081; MrdA_transpept; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02081};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02081};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02081};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02081};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02081};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02081}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
FT DOMAIN 64..238
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 271..610
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 631..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02081"
SQ SEQUENCE 654 AA; 71758 MW; 0086B9EFF146BF71 CRC64;
MAYSNELKNH QNELHHFRLR LTVLGFLVLI AFSVLVSRFY FLQINRYDYY QTLAENNRIS
IVPIAPNRGL ITDRNGVVLA HNFFVYTLEI TPSKIADLES TIAELAQLVE INSVDLKRFK
KLKAQSHSFE SVPIRTHLNE VEAAKFAVNR YRFPGVEIKS RLFRHYPNGK MGAHMIGYIG
RINDKDLVKL AENDVLSNYK GSDHIGKTGI EQSYEAELHG TTGFQQVEID ADGKAVRVLS
STAPVSGNNL VLSADIKLQE IAETAFGERR GALVAIKPST GEVLAFVSMP TFDSNLFVDG
IDTENWKLLN ESLDKPLINR PLRGIYPPGS TFKPFTALAG LEAGKREPPF SISDAGYFML
PNSSHRYRDW KPGGHGNVDM RRAITISCDT FFYGLAIELG IEKLTDFVRH FGFGQKSGID
IAGEVSGLLP TPEWKQRRFK QPWYKGETVI VGIGQGYTLA TPMQLAQATA ILANKGVAMR
PHLVSSITNS KTGISKVSTT VVNNTINLKD KNLEIVNLGM IDVTLPGGTA ASVGANAGYS
IAAKTGTAQV IGIKQNEKYN ERLVNERHRD HALFIAYAPA ENPTIALAVI VENGGHGGSA
AGPIARKVMD YYLLGKLPAV DIPKDAKPLP LATNNAAAGA SQPIENAPEE EHYD
//
